Nuclear magnetic resonance spectroscopy

Nuclear magnetic resonance spectroscopy, also known as NMR spectroscopy, is a research technique that exploits the magnetic properties of certain atomic nuclei.

NMR is used in biomolecular systems among others.

  • Insights into closed enzymes

    Representation of electron density at the disulphide bond (yellow, between C56 and C163) and in its close vicinity. Prof. Michael Kovermann, University of Konstanz

    Scientists at the University of Konstanz and Umeå University in Sweden have arrived at a structural model of the enzyme adenylate kinase in its closed state.

    The adenylate kinase enzyme is crucial to managing the energy budget of cells, accelerating the biochemical process whereby energy is stored or released. The enzyme continuously changes between open and closed states. In its closed form, adenylate kinase is particularly active biochemically and thus able to accelerate the chemical reaction of “docked” molecules that it has encased like a clam. These are called ligands.

  • News About Drug Delivery

    As the loading with curcumin (yellow) increases, the dissolution rate of the containers made of polymeric micelles (blue) decreases. (Picture: Ann-Christin Pöppler)

    Nanocontainer for drugs can have their pitfalls: If they are too heavily loaded, they will only dissolve poorly. Why this happens is now reported by a Würzburg research group in "Angewandte Chemie". Nanocapsules and other containers can transport drugs through a patient's body directly to the origin of the disease and release them there in a controlled manner. Such sophisticated systems are occasionally used in cancer therapy. Because they work very specifically, they have fewer side effects than drugs that are distributed throughout the entire organism.

  • Superfast Insights Into Cellular Events

    Frankfurt researchers followed the movements of this tiny molecule – just two-thousandths of the thickness of a piece of paper. The RNA aptamer changes its structure when it binds hypoxanthine. Goethe University

    FRANKFURT. Even more detailed insights into the cell will be possible in future with the help of a new development in which Goethe University was involved: Together with scientists from Israel, the research group led by Professor Harald Schwalbe has succeeded in accelerating a hundred thousand-fold the nuclear magnetic resonance (NMR) method for investigating RNA. In the same way that a single piece of a puzzle fits into the whole, the molecule hypoxanthine binds to a ribonucleic acid (RNA) chain, which then changes its three-dimensional shape within a second and in so doing triggers new processes in the cell. Thanks to an improved method, researchers are now able to follow almost inconceivably tiny structural changes in cells as they progress – both in terms of time as well as space. The research group led by Professor Harald Schwalbe from the Center for Biomolecular Magnetic Resonance (BMRZ) at Goethe University has succeeded, together with researchers from Israel, in accelerating a hundred thousand-fold the nuclear magnetic resonance (NMR) method for investigating RNA.